A novel targeted multi-functional fusion protein possesses inhibitory activities against bacteria, thrombin and platelet aggregation.
Gao. Jiange J; Hu. Zongli Z; Zhao. Zhiping Z; Liu. Guanglei G; Ren. Yanrong Y; Chen. Guoping G
Key Findings
- A fusion protein (LHAD) combining LL‑37, a thrombin‑recognition peptide, hirudin fragment, AAP, and RGD was successfully produced in yeast.
- The LHAD protein showed antibacterial activity in vitro.
- LHAD demonstrated anti‑platelet aggregation and stronger anti‑thrombin activity than natural hirudin.
Practical Outcomes
- The study suggests it’s possible to create multi‑functional molecules that both fight infection and reduce clotting, but it’s still far from a consumer product. No dosage, safety, or real‑world protocol is provided, so biohackers can’t apply it directly yet.
Summary
Scientists built a new protein that mixes the antimicrobial peptide LL‑37 with pieces that block clotting and platelet clumping. In lab tests it killed bacteria, stopped platelets from sticking together, and was better at stopping thrombin (a clotting enzyme) than natural hirudin. It’s an early‑stage, lab‑only result, not a ready‑to‑use supplement or treatment.
Abstract
In the present study, we designed a novel targeted multi-functional fusion protein LHAD composed of LL-37, FXa recognition peptide, hirudin-12-residue, AAP, and RGD peptide. It was expressed in the Pichia pastoris GS115 strain and purified by affinity chromatography. The in vitro studies suggested that the novel designed protein exhibited antibacterial activity, anti-platelet aggregation and anti-thrombin activities. Moreover, the capability of anti-thrombin was significantly increased compared to that of natural hirudin. Our study may provide a potential approach to design multi-functional drugs for the prevention and management of thrombosis.
Study Information
pubmed
2011
2011-09-30T00:00:00.000Z
10.1007/s10930-011-9357-6
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